Evidence that in vivo estradiol receptor translocated into nuclei is dephosphorylated and released into cytoplasm

F. Auricchio, A. Migliaccio, G. Castoria, S. Lastoria, A. Rotondi

Research output: Contribution to journalArticle


Most of the estradiol binding activity is lost after the receptor-hormone complex migrates into the nuclei. We report that at the same time an equivalent amount of receptor unable to bind hormone appears in cytosol. ATP incubated with uterine cytosol from 17β-estradiol injected mice causes an increase in hormone binding activity. This activation is catalyzed by the ATP-dependent enzyme which reactivates hormone binding of estradiol receptor previously inactivated by a nuclear phosphatase (1). The inactive receptor retains the property to be activated by the ATP-dependent enzyme after a partial purification by heparin-Sepharose. A large dose of cycloheximide does not inhibit the appearance of ATP-activated cytosol receptor. Apparently the 17β-estradiol receptor which migrates into the nucleus is inactivated by the nuclear phosphatase and then released in an inactive, dephosphorylated form into the cyoplasm.

Original languageEnglish
Pages (from-to)149-157
Number of pages9
JournalBiochemical and Biophysical Research Communications
Issue number1
Publication statusPublished - May 14 1982


ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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